Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Conformational Plasticity of Hepatitis B Core Protein Spikes Promotes Peptide Binding Independent of the Secretion Phenotype.
Journal, issue, pages	Microorganisms, Vol. 9, Issue 5, Year 2021
Publish date	Apr 29, 2021
Authors	Cihan Makbul / Vladimir Khayenko / Hans Michael Maric / Bettina Böttcher /
PubMed Abstract	Hepatitis B virus is a major human pathogen, which forms enveloped virus particles. During viral maturation, membrane-bound hepatitis B surface proteins package hepatitis B core protein capsids. This ...Hepatitis B virus is a major human pathogen, which forms enveloped virus particles. During viral maturation, membrane-bound hepatitis B surface proteins package hepatitis B core protein capsids. This process is intercepted by certain peptides with an "LLGRMKG" motif that binds to the capsids at the tips of dimeric spikes. With microcalorimetry, electron cryo microscopy and peptide microarray-based screens, we have characterized the structural and thermodynamic properties of peptide binding to hepatitis B core protein capsids with different secretion phenotypes. The peptide "GSLLGRMKGA" binds weakly to hepatitis B core protein capsids and mutant capsids with a premature (F97L) or low-secretion phenotype (L60V and P5T). With electron cryo microscopy, we provide novel structures for L60V and P5T and demonstrate that binding occurs at the tips of the spikes at the dimer interface, splaying the helices apart independent of the secretion phenotype. Peptide array screening identifies "SLLGRM" as the core binding motif. This shortened motif binds only to one of the two spikes in the asymmetric unit of the capsid and induces a much smaller conformational change. Altogether, these comprehensive studies suggest that the tips of the spikes act as an autonomous binding platform that is unaffected by mutations that affect secretion phenotypes.
External links	Microorganisms / PubMed:33946808 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 3.2 Å
Structure data	12810 7oco EMDB-12810, PDB-7oco: Hepatitis B core protein -low secretion phenotype L60V Method: EM (single particle) / Resolution: 3.2 Å 12815 7ocw EMDB-12815, PDB-7ocw: Hepatitis B core protein -low secretion phenotype P5T Method: EM (single particle) / Resolution: 3.2 Å 12819 7od4 EMDB-12819: Hepatitis B core protein PDB-7od4: Hepatitis B core protein. Method: EM (single particle) / Resolution: 2.8 Å 12820 7od6 EMDB-12820, PDB-7od6: Hepatitis B core protein + GSLLGRMKGA Method: EM (single particle) / Resolution: 3.0 Å 12821 7od7 EMDB-12821, PDB-7od7: Hepatitis B core protein + SLLGRM Method: EM (single particle) / Resolution: 2.8 Å 12822 7od8 EMDB-12822, PDB-7od8: Hepatitis B core Protein mutant L60V + GSLLGRMKGA Method: EM (single particle) / Resolution: 3.0 Å 12823 7oew EMDB-12823: Hepatitis B core protein capsid, mutant F97L with bound MHRSLLGRMKGA PDB-7oew: Hepatitis B core protein mutant F97L with bound MHRSLLGRMKGA Method: EM (single particle) / Resolution: 2.9 Å 12824 7oev EMDB-12824: Hepatitis B core Protein, F97L - premature secretion mutant with bound GSLLGRMKGA PDB-7oev: Hepatitis B core protein mutant F97L with bound GSLLGRMKGA Method: EM (single particle) / Resolution: 3.1 Å 12825 7oen EMDB-12825: Hepatitis B core protein with low secretion phenotype (P5T) and bound GSLLGRMKGA PDB-7oen: Hepatitis B core protein mutant P5T with bound GSLLGRMKGA Method: EM (single particle) / Resolution: 3.2 Å
Source	hepatitis b virus genotype d subtype ayw (isolate france/tiollais/1979) hepatitis b virus synthetic construct (others)
Keywords	VIRUS LIKE PARTICLE / low secretion phenotype / L60V / Hepatitis B core protein / P5T / inhibitory peptide / Hepatitis B virus / peptide inhibitor / premature envelopment mutant / F97L / GSLLGRMKGA / MHRSLLGRMKGA